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Literature summary for 2.7.7.12 extracted from
- The structural and molecular biology of type I galactosemia: enzymology of galactose 1-phosphate uridylyltransferase (2011), IUBMB Life, 63, 694-700.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme might be a target for inhibitor design in galactosemia treatment | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure determination and analysis | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP | - |
Homo sapiens |  |
| ADP-glucose | - |
Homo sapiens | |
| alpha-D-galactose 1-phosphate | competitive substrate inhibition in the forward reaction | Escherichia coli | |
| alpha-D-galactose 1-phosphate | competitive substrate inhibition in the forward reaction | Homo sapiens | |
| ATP | - |
Homo sapiens | |
| CDP-glucose | - |
Homo sapiens | |
| diethyl dicarbonate | inactivates the enzyme, reversable by hydroxylamine | Escherichia coli | |
| GDP-glucose | - |
Homo sapiens | |
| TDP-glucose | - |
Homo sapiens | |
| UDP | - |
Homo sapiens | |
| UDP-galactose | the product of the forward reaction is a competitive inhibitor with respect to UDP-glucose and a mixed inhibitor with respect to galactose 1-phosphate | Escherichia coli | |
| UDP-galactose | the product of the forward reaction is a competitive inhibitor with respect to UDP-glucose and a mixed inhibitor with respect to galactose 1-phosphate | Homo sapiens | |
| UDP-glucuronic acid | - |
Homo sapiens | |
| UDP-mannose | - |
Homo sapiens | |
| UDP-xylose | - |
Homo sapiens | |
| UMP | - |
Homo sapiens | |
| Uracil | - |
Homo sapiens | |
| uridine | - |
Homo sapiens | |
| UTP | - |
Homo sapiens | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | the enzyme homodimer contains one zinc (II) and one iron (II) ion per subunit, pyramidial iron-binding site, structure, overview | Escherichia coli | |
| Zn2+ | the enzyme homodimer contains one zinc (II) and one iron (II) ion per subunit, tetrahedral zinc binding site, structure, overview | Escherichia coli | |
| Zn2+ | the zinc co-orientating residues are not conserved and therefore, it may only bind one metal ion per monomer | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate | Escherichia coli | - |
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose | - |
r | |
| UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate | Homo sapiens | - |
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose | ping-pong catalytic mechanism, a UMP group is transferred from UDP-glucose to His186 in the active site of the enzyme, overview | Homo sapiens | |
| UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose | ping-pong catalytic mechanism, overview. A UMP group is transferred from UDP-glucose to His166 in the active site of the enzyme | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme has a strict requirement for UDP-glucose or UDP-galactose as substrates, while GDP-glucose, ADP-glucose, TDP-glucose, CDP-glucose, UDPxylose, and UDP-mannose are all unable to support activity | Escherichia coli | ? | - |
? | |
| additional information | the enzyme has a strict requirement for UDP-glucose or UDP-galactose as substrates, while GDP-glucose, ADP-glucose, TDP-glucose, CDP-glucose, UDPxylose, and UDP-mannose are all unable to support activity | Homo sapiens | ? | - |
? | |
| UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate | - |
Escherichia coli | alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose | - |
r | |
| UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate | - |
Homo sapiens | alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| galactose 1-phosphate uridylyltransferase | - |
Escherichia coli |
| galactose 1-phosphate uridylyltransferase | - |
Homo sapiens |
| GALT | - |
Escherichia coli |
| GALT | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | GALT belongs to the histidine triad family of transferases | Escherichia coli |
| evolution | GALT belongs to the histidine triad family of transferases | Homo sapiens |
| malfunction | reduced galactose 1-phosphate uridylyltransferase activity is associated with the genetic disease type I galactosemia. Enzyme-deficiency results in an increase in the cellular concentration of galactose 1-phosphate. The accumulation of this toxic metabolite, combined with aberrant glycoprotein and glycolipid biosynthesis, is likely to be the major factor in molecular pathology | Homo sapiens |
| metabolism | the enzyme catalyzes a critical step in the Leloir pathway, overview | Escherichia coli |
| metabolism | the enzyme catalyzes a critical step in the Leloir pathway, overview | Homo sapiens |
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